ID A0A0S8FMJ8_9GAMM Unreviewed; 318 AA.
AC A0A0S8FMJ8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=AMJ59_01935 {ECO:0000313|EMBL:KPK61394.1};
OS Gammaproteobacteria bacterium SG8_31.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK61394.1, ECO:0000313|Proteomes:UP000051321};
RN [1] {ECO:0000313|EMBL:KPK61394.1, ECO:0000313|Proteomes:UP000051321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_31 {ECO:0000313|EMBL:KPK61394.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK61394.1}.
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DR EMBL; LJTI01000002; KPK61394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8FMJ8; -.
DR PATRIC; fig|1703405.3.peg.3767; -.
DR Proteomes; UP000051321; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR041107; Rimk_N.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF2; COENZYME GAMMA-F420-2:ALPHA-L-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF18030; Rimk_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 115..299
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 318 AA; 35266 MW; B1BC2FABFB698D95 CRC64;
MKYAATGWIL WRPDPSLVKQ ESYEIDRLLE AAPEHAYQVE VVNPDDVQLL VNSEKEDGIF
VNGDKVKLPD FVIPRMGSTT NYFSLAVLRQ LENLGVYCLN GSAAVELARD KLLHLQLLAN
AGLPVPKTIL VQFPVNADFV ETEMGFPVVV KTLVGTQGSG VYLCENRENL VDMLQFVEAN
NPSAQLILQQ FLSESRGRDV RVVSIGGHIV AAMERIAKSG FKSNYSQGGE ARPFEYGHRN
ELSVAEVMRI LDMDIAGLDF LYDEEVGFRI CEVNSSPGFE GLEATCGVDV PAFIYEYLDV
KFRISRKAKA RLLGQTPG
//
